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2mlt

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==MELITTIN==
==MELITTIN==
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<StructureSection load='2mlt' size='340' side='right' caption='[[2mlt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='2mlt' size='340' side='right'caption='[[2mlt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2mlt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mlt 1mlt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MLT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2mlt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mlt 1mlt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MLT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mlt RCSB], [http://www.ebi.ac.uk/pdbsum/2mlt PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlt OCA], [https://pdbe.org/2mlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mlt RCSB], [https://www.ebi.ac.uk/pdbsum/2mlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MEL_APIME MEL_APIME]] Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.<ref>PMID:20472009</ref> Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.<ref>PMID:20472009</ref>
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[https://www.uniprot.org/uniprot/MEL_APIME MEL_APIME] Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.<ref>PMID:20472009</ref> Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.<ref>PMID:20472009</ref>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Apis mellifera]]
[[Category: Apis mellifera]]
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[[Category: Eisenberg, D]]
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[[Category: Large Structures]]
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[[Category: Gribskov, M]]
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[[Category: Eisenberg D]]
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[[Category: Terwilliger, T C]]
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[[Category: Gribskov M]]
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[[Category: Terwilliger TC]]

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MELITTIN

PDB ID 2mlt

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